Results 281 to 290 of about 365,538 (313)
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Crystal structure of the catalytic domain of a thermophilic endocellulase

Biochemistry, 1993
One way to improve the economic feasibility of biomass conversion is to enhance the catalytic efficiency of cellulases through protein engineering. This requires that high-resolution structures of cellulases be available. Here we present the structure of E2cd, the catalytic domain of the thermophilic endocellulase E2 from Thermomonospora fusca, as ...
M, Spezio, D B, Wilson, P A, Karplus
openaire   +2 more sources

Catalytic and Regulatory Domains of Doublecortin Kinase-1

Biochemistry, 2003
Doublecortin kinase-1 (DCK1) is a newly described multidomain protein kinase with a sequence significantly similar to those of both CaM kinases (CaMKs) and doublecortin, the product of the gene mutated in X-linked lissencephaly/double cortex syndrome, a severe developmental disorder of the nervous system.
Limin, Shang   +4 more
openaire   +2 more sources

Structure of the Isolated Catalytic Domain of Diphtheria Toxin

Biochemistry, 1995
The structure of the isolated catalytic domain of diphtheria toxin at pH 5.0 was determined by X-ray crystallography at 2.5 A resolution and refined to an R-factor of 19.7%. The domain is bound to its endogenous inhibitor adenylyl(3'-->5')uridine 3'-monophosphate (ApUp). The structure of this 190-residue domain, which was expressed in and isolated from
M S, Weiss   +3 more
openaire   +2 more sources

Structural analysis of the catalytic domain of tetanus neurotoxin

Toxicon, 2005
Clostridium neurotoxins, comprising the tetanus neurotoxin and the seven antigenically distinct botulinum neurotoxins (BoNT/A-G), are among the known most potent bacterial protein toxins to humans. Although they have similar function, sequences and three-dimensional structures, the substrate specificity and the selectivity of peptide bond cleavage are ...
Krishnamurthy N, Rao   +3 more
openaire   +2 more sources

Involvement of tryptophans at the catalytic and subunit-binding domains of transcarboxylase

Biochemistry, 1988
Transcarboxylase from Propionibacterium shermanii is a multisubunit enzyme. It consists of one central hexameric subunit to which six outer dimeric subunits are attached through twelve biotinyl subunits. Both the central and the outer subunits are multi-tryptophan (Trp) proteins, and each contains 5 Trps per monomer.
G K, Kumar, H, Beegen, H G, Wood
openaire   +2 more sources

Zinc Content of Promatrilysin, Matrilysin and the Stromelysin Catalytic Domain

Biochemical and Biophysical Research Communications, 1994
Promatrilysin expressed in Escherichia coli and Chinese hamster ovary cells contains 2.36 +/- 0.19 and 2.13 +/- 0.39 moles of zinc per mole of protein, respectively, while the activated enzyme contains 2.22 +/- 0.21. The catalytic domain of stromelysin-1 expressed in E. coli contains 2.22 +/- 0.11. Thus these matrix metalloproteinases contain two metal
D, Soler   +6 more
openaire   +2 more sources

Expression and Characterization of the Catalytic Domain of Human Phenylalanine Hydroxylase

Archives of Biochemistry and Biophysics, 1997
A truncated version of human phenylalanine hydroxylase which contains the carboxy terminal 336 amino acids was produced in Escherichia coli. It was purified by ammonium sulfate precipitation, Q-Sepharose chromatography, and hydroxyapatite chromatography.
S C, Daubner   +2 more
openaire   +2 more sources

Virtual screening of natural compounds as selective inhibitors of polo-like kinase-1 at C-terminal polo box and N-terminal catalytic domain

Journal of Biomolecular Structure and Dynamics, 2022
Femi Olawale   +2 more
exaly  

Designing graded catalytic domain to homogenize temperature distribution while dry reforming of CH4

International Journal of Hydrogen Energy, 2018
Atsushi Kubota   +2 more
exaly  

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